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ID EDD_RAT STANDARD; PRT; 920 AA.
AC Q62671;
DT 01-NOV-1997 (Rel. 35, Created)
DT 15-JUN-2002 (Rel. 41, Last sequence update)
DT 15-JUN-2002 (Rel. 41, Last annotation update)
DE Ubiquitin--protein ligase EDD (EC 6.3.2.-) (Hyperplastic discs
DE protein homolog) (100 kDa protein) (Fragment).
GN EDD OR HYD.
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
RN [1]
RP SEQUENCE FROM N.A.
RC STRAIN=Wistar; TISSUE=Testis;
RA Mueller D., Rehbein M., Baumeister H., Richter D.;
RT "Molecular characterization of a novel rat protein structurally
RT related to poly(A) binding proteins and the 70K protein of the U1
RT small nuclear ribonucleoprotein particle (snRNP).";
RL Nucleic Acids Res. 20:1471-1475(1992).
RN [2]
RP ERRATUM.
RA Mueller D., Rehbein M., Baumeister H., Richter D.;
RL Nucleic Acids Res. 20:2624-2624(1992).
RN [3]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R.,
RA Sutherland R.L., Watts C.K.W.;
RT "Identification of a human HECT family protein with homology to the
RT Drosophila tumor suppressor gene hyperplastic discs.";
RL Oncogene 17:3479-3491(1998).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC then directly transfers the ubiquitin to targeted substrates (By
CC similarity). May be involved in maturation and/or post-
CC transcriptional regulation of mRNA. May play a role in control of
CC cell cycle progression. May have tumor suppressor function.
CC Regulates DNA topoisomerase II binding protein (TopBP1) for the
CC DNA damage response (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear (By similarity).
CC -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present
CC in liver, kidney, lung and brain.
CC -!- DEVELOPMENTAL STAGE: In early post-natal life, expression in
CC the testis increases to reach a maximum around day 28.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
CC thiolester formation.
CC -!- SIMILARITY: CONTAINS 1 HECT-TYPE E3 UBIQUITIN-PROTEIN LIGASE
CC DOMAIN.
CC -!- CAUTION: Ref.1 sequence differs from that shown due to a
CC frameshift in position 30.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X64411; CAA45756.1; ALT_FRAME.
DR HSSP; O95071; 1I2T.
DR InterPro; IPR000569; HECT_domain.
DR InterPro; IPR002004; PABP/HECT.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR PROSITE; PS50237; HECT; 1.
KW Ubl conjugation pathway; Ligase; Nuclear protein.
FT NON_TER 1 1
FT DOMAIN 515 571 PABP-LIKE.
FT DOMAIN 583 920 HECT.
FT DOMAIN 108 119 ASP/GLU-RICH (ACIDIC).
FT DOMAIN 158 181 PRO-RICH.
FT DOMAIN 451 470 ARG/GLU-RICH (MIXED CHARGE).
FT DOMAIN 479 488 ARG/ASP-RICH (MIXED CHARGE).
FT DOMAIN 610 621 ASP/GLU-RICH (ACIDIC).
FT DOMAIN 858 878 PRO-RICH.
FT BINDING 889 889 UBIQUITIN (BY SIMILARITY).
SQ SEQUENCE 920 AA; 103949 MW; 465771084536C3AA CRC32;
ARRERMTARE EASLRTLEGR RRATLLSARQ GMMSARGDFL NYALSLMRSH NDEHSDVLPV
LDVCSLKHVA YVFQALIYWI KAMNQQTTLD TPQLERKRTR ELLELGIDNE DSEHENDDDT
SQSATLNDKD DESLPAETGQ NHPFFRRSDS MTFLGCIPPN PFEVPLAEAI PLADQPHLLQ
PNARKEDLFG RPSQGLYSSS AGSGKCLVEV TMDRNCLEVL PTKMSYAANL KNVMNMQNRQ
KKAGEDQSML AEEADSSKPG PSAHDVAAQL KSSLLAEIGL TESEGPPLTS FRPQCSFMGM
VISHDMLLGR WRLSLELFGR VFMEDVGAEP GSILTELGGF EVKESKFRRE MEKLRNQQSR
DLSLEVDRDR DLLIQQTMRQ LNNHFGRRCA TTPMAVHRVK VTFKDEPGEG SGVARSFYTA
IAQAFLSNEK LPNLDCIQNA NKGTHTSLMQ RLRNRGERDR EREREREMRR SSGLRAGSRR
DRDRDFRRQL SIDTRPFRPA SEGNPSDDPD PLPAHRQALG ERLYPRVQAM QPAFASKITG
MLLELSPAQL LLLLASEDSL RARVEEAMEL IVAHGRENGA DSILDLGLLD SSEKVQENRK
RHGSSRSVVD MDLDDTDDGD DNAPLFYQPG KRGFYTPRPG KNTEARLNCF RNIGRILGLC
LLQNELCPIT LNRHVIKVLL GRKVNWHDFA FFDPVMYESL RQLILASQSS DADAVFSAMD
LAFAVDLCKE EGGGQVELIP NGVNIPVTPQ NVYEYVRKYA EHRMLVVAEQ PLHAMRKGLL
DVLPKNSLED LTAEDFRLLV NGCGEVNVQM LISFTSFNDE SGENAEKLLQ FKRWFWSIVE
RMSMTERQDL VYFWTSSPSL PASEEGFQPM PSITIRPPDD QHLPTANTCI SRLYVPLYSS
KQILKQKLLL AIKTKNFGFV
//
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